Mouse Anti-Human C1qR1/CD93 Antibody (VIMD)

C1qR1, also known as CD93, is a type I transmembrane glycoprotein primarily expressed on the surface of myeloid cells, endothelial cells, platelets, and hematopoietic stem cells. This protein was initially identified as a receptor for complement C1q, but subsequent studies have suggested that its binding to C1q may only occur under non-physiological conditions, and its more core functional roles involve cell–cell adhesion, clearance of apoptotic cells, and maintenance of plasma cells within the bone marrow niche. As a highly glycosylated protein, the molecular weight of C1qR1 is considerably higher than its predicted value based on amino acid sequence (approximately 66 kDa), with an observed apparent molecular weight of 120–140 kDa in experiments. Its structure comprises a C-type lectin-like domain responsible for ligand binding and multiple epidermal growth factor-like domains, and its cytoplasmic tail can interact with moesin—a cytoskeleton-linking protein—participating in cytoskeletal remodeling. Due to its expression profile and functional characteristics, C1qR1 not only serves as a marker for various cell types but also represents an important molecule in regulating innate immune responses and hematopoietic homeostasis.